Any feedback?
Information on EC 2.1.3.6 - putrescine carbamoyltransferase and Organism(s) Enterococcus faecalis and UniProt Accession Q837U7
for references in articles please use BRENDA:EC2.1.3.6Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.1.3.6 putrescine carbamoyltransferaseIUBMB Comments
The plant enzyme also catalyses the reactions of EC 2.1.3.3 ornithine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC 3.5.3.12 agmatine deiminase, thus acting as putrescine synthase, converting agmatine [(4-aminobutyl)guanidine] and ornithine into putrescine and citrulline, respectively.
Specify your search results
Word Map
The taxonomic range for the selected organisms is: Enterococcus faecalis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
putrescine carbamoyltransferase, ptcase, putrescine transcarbamylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PTCase
putrescine synthase
-
-
-
-
putrescine transcarbamylase
PTCase
-
-
-
-
putrescine transcarbamylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
transfer of carbamoyl phosphate
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
carbamoyl-phosphate:putrescine carbamoyltransferase
The plant enzyme also catalyses the reactions of EC 2.1.3.3 ornithine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC 3.5.3.12 agmatine deiminase, thus acting as putrescine synthase, converting agmatine [(4-aminobutyl)guanidine] and ornithine into putrescine and citrulline, respectively.
CAS REGISTRY NUMBER
COMMENTARY
9076-55-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
carbamoyl phosphate + L-ornithine
phosphate + N-carbamoyl-L-ornithine
-
low activity, reaction of EC 2.1.3.3
-
-
?
carbamoyl phosphate + ornithine
phosphate + N-carbamoylornithine
-
only weak activity with ornithine as a substrate
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
-
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
substrate binding structures, overview
-
-
?
arsenate + N-carbamoylputrescine
?
-
carbamoyl arsenate as intermediate is not formed
-
-
ir
carbamoyl phosphate + 1,3-diaminopropane
phosphate + N1-carbamoyl-1,3-diaminopropane
-
-
-
?
carbamoyl phosphate + 1,3-diaminopropane
phosphate + N1-carbamoyl-1,3-diaminopropane
-
-
-
-
?
carbamoyl phosphate + 1,6-diaminohexane
phosphate + N1-carbamoyl-1,6-diaminohexane
-
-
-
?
carbamoyl phosphate + 1,6-diaminohexane
phosphate + N1-carbamoyl-1,6-diaminohexane
-
-
-
-
?
carbamoyl phosphate + cadaverine
phosphate + N-carbamoylcadaverine
-
-
-
?
carbamoyl phosphate + cadaverine
phosphate + N-carbamoylcadaverine
-
-
-
-
?
carbamoyl phosphate + cadaverine
phosphate + N-carbamoylcadaverine
-
only weak activity with cadaverine a substrate
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
phosphorolysis of N-carbamoylputrescine is possibly the physological role of the enzyme
r
carbamoyl phosphate + spermidine
phosphate + N-carbamoylspermidine
-
-
-
?
carbamoyl phosphate + spermidine
phosphate + N-carbamoylspermidine
-
-
-
-
?
carbamoyl phosphate + spermine
phosphate + N-carbamoylspermine
-
-
-
?
carbamoyl phosphate + spermine
phosphate + N-carbamoylspermine
-
-
-
-
?
additional information
?
-
in addition to using putrescine, the enzyme can utilize L-ornithine as a poor substrate, see EC 2.1.3.3. Differences between the respective 230 and SMG loops of PTC and OTC appear to account for the differential preference of these enzymes for putrescine and ornithine, active center and the discrimination mechanism between putrescine and ornithine, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the second of three steps of ATP synthesis from agmatine
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
carbamoyl phosphate + L-ornithine
phosphate + N-carbamoyl-L-ornithine
-
low activity, reaction of EC 2.1.3.3
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
-
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
phosphorolysis of N-carbamoylputrescine is possibly the physological role of the enzyme
r
additional information
?
-
-
the enzyme catalyzes the second of three steps of ATP synthesis from agmatine
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-(phosphonoacetyl)-putrescine
-
i.e. PAPU, highly potent and selective inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.101
Carbamoyl phosphate
pH and temperature not specified in the publication
0.136
putrescine
pH and temperature not specified in the publication
32.9
putrescine
recombinant PTC mutant Y230V/G231S/L232M/Y233G, pH 8.5, 37°C
additional information
additional information
in contrast to other trimeric carbamoyltransferases, PTCase binds both carbamoyl phosphate and putrescine with Hill coefficients at saturating concentrations of the other substrate of 1.53 and 1.80, respectively
-
additional information
additional information
-
in contrast to other trimeric carbamoyltransferases, PTCase binds both carbamoyl phosphate and putrescine with Hill coefficients at saturating concentrations of the other substrate of 1.53 and 1.80, respectively
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.13
recombinant PTC mutant Y230V/G231S/L232M/Y233G, substrate putrescine, pH 8.5, 37°C
813
recombinant wild-type PTC, substrate putrescine, pH 8.5, 37°C
460
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme generates carbamoyl phosphate for ATP production in the fermentative catabolism of agmatine
additional information
additional information
sequence 230YGLY233 is the putrescine signature sequence
additional information
the C-terminal helix is essential for both formation of the functional trimer and catalytic activity, since truncated PTCase without the C-terminal helix aggregates and has only 3% of native catalytic activity. Active site structure, overview
additional information
-
the C-terminal helix is essential for both formation of the functional trimer and catalytic activity, since truncated PTCase without the C-terminal helix aggregates and has only 3% of native catalytic activity. Active site structure, overview
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
PTCase also has a unique structural feature: a long C-terminal helix that interacts with the adjacent subunit to enhance intersubunit interactions in the molecular trimer. The C-terminal helix os essential for both formation of the functional trimer and catalytic activity, since truncated PTCase without the C-terminal helix aggregates and has only 3% of native catalytic activity
trimer
additional information
additional information
presence or absence of supratrimeric oligomerization, structure comparison and analysis, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified full-length PTC or in complex with inhibitors N-(phosphonoacetyl)-putrescine or N-(phosphonoacetyl)-L-ornithine, and trunacted PTC in complex with N-(phosphonoacetyl)-L-ornithine, hanging drop vapor diffusion technique, mixing of 0.001 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5 containing 0.43 mM ligand with 0.001 ml of crystallization solution composed of 125 mM (NH4)2SO4, 17% PEG 3350, 0.1 M Bis-Tris, pH 5.5, 21°C, X-ray diffraction structure determination and analysis at 2.5 A, 2.0 A, and 1.59 A resolution, respectively, modeling
purified His-tagged wild-type PTCase, from a solution containing 200 mM magnesium sulfate, 15-17% w/v PEG 3350, 100 mM Bis-tris, pH 5.5, soaking in mother liquor containing 25% v/v ethylene glycol for 1 min for cryoprotection, X-ray diffraction structure determination and analysis at 3.2 A resolution
purified recombinant enzyme in presence of inhibitor N-(phosphonoacetyl)-putrescine, X-ray diffraction structure determination and analysis at 3.0 A resolution
-
using the sparse-matrix sampling vapor-diffusion method. The addition of N-(phosphonoacetyl)-putrescine to the crystallization drop strongly improves the results of the crystallization
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R54G
site-directed mutagenesis, inactive mutant, not exhibiting any PTC or OTC activity
Y230V/G231S/L232M/Y233G
engineering of the 230-loop of PTC, by replacing the sequence 230YGLY233 of the putrescine signature by its OTC counterpart VSMG, favors the use of ornithine and impairs that of putrescine
additional information
confirmation of decreased stability of the trimer of PTC lacking the C-terminal helix by deleting this helix
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
-
carbamoylphosphate, diphosphate, ornithine, 2,4-diaminobutyrate and norvaline protect against denaturation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 2.5 mg/ml, 50 mM potassium phosphate, pH 7.5, 3 years, no loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged protein from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, and gel filtration
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene agcB, expression as His-tagged protein in Escherichia coli strain BL21(DE3)
gene ef0732, gene cluster organization, DNA and amino acid sequence determination and analysis, overexpression of His-tagged enzyme in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Roon, R.J.; Barker, H.A.
Fermentation of agmatine in Streptococcus faecalis: occurence of putrescine transcarbamoylase
J. Bacteriol.
109
44-50
1972
Enterococcus faecalis, Enterococcus faecalis 10C1
Stalon, V.
Putrescine carbamoyltransferase (Streptococcus faecalis)
Methods Enzymol.
94
339343
1983
Enterococcus faecalis, Pediococcus acidilactici
-
Wargnies, B.; Lauwers, N.; Stalon, V.
Structure and properties of the putrescine carbamoyltransferase of Streptococcus faecalis
Eur. J. Biochem.
101
143-12
1979
Enterococcus faecalis
Llacer, J.L.; Polo, L.M.; Tavarez, S.; Alarcon, B.; Hilario, R.; Rubio, V.
The gene cluster for agmatine catabolism of Enterococcus faecalis: study of recombinant putrescine transcarbamylase and agmatine deiminase and a snapshot of agmatine deiminase catalyzing its reaction
J. Bacteriol.
189
1254-1265
2007
Enterococcus faecalis, Enterococcus faecalis ATCC 700802
Polo, L.M.; Gil-Ortiz, F.; Cantin, A.; Rubio, V.
New insight into the transcarbamylase family: the structure of putrescine transcarbamylase, a key catalyst for fermentative utilization of agmatine
PLoS ONE
7
e31528
2012
Enterococcus faecalis (Q837U7)
Shi, D.; Yu, X.; Zhao, G.; Ho, J.; Lu, S.; Allewell, N.M.; Tuchman, M.
Crystal structure and biochemical properties of putrescine carbamoyltransferase from Enterococcus faecalis: assembly, active site, and allosteric regulation
Proteins
80
1436-1447
2012
Enterococcus faecalis (Q837U7), Enterococcus faecalis, Enterococcus faecalis ATCC 700802 (Q837U7)
EXTERNAL LINKS (specific for EC-Number 2.1.3.6)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
